ENZYME entry: EC 1.20.4.1

Accepted Name
Arsenate reductase (glutaredoxin).
Reaction catalysed
Arsenate + glutaredoxin <=> arsenite + glutaredoxin disulfide + H(2)O
Cofactor(s)
Molybdenum.
Comment(s)
  • The glutaredoxins catalyze glutathione-disulfide oxidoreductions and have a redox-active disulfide/dithiol in the active site (-Cys- Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized form.
  • Glutaredoxins have a binding site for glutathione, which is required to reduce them to the dithiol form.
  • Thioredoxins reduced by NADPH and thioredoxin reductase can act as alternative substrates.
  • The enzyme is part of a system for detoxifying arsenate.
  • Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16.
  • In other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway to non-toxic organoarsenical compounds.
  • Formerly EC 1.97.1.5.
Cross-references
BRENDA1.20.4.1
EC2PDB1.20.4.1
ExplorEnz1.20.4.1
PRIAM enzyme-specific profiles1.20.4.1
KEGG Ligand Database for Enzyme Nomenclature1.20.4.1
IUBMB Enzyme Nomenclature1.20.4.1
IntEnz1.20.4.1
MEDLINEFind literature relating to 1.20.4.1
MetaCyc1.20.4.1
UniProtKB/Swiss-Prot
Q336V5, ACR21_ORYSJ;  Q10SX6, ACR22_ORYSJ;  P08692, ARSC1_ECOLX;  
P52147, ARSC2_ECOLX;  P0CF87, ARSCL_ECOLI;  O50595, ARSC_ACIMA;  
P0AB96, ARSC_ECOLI;  P44589, ARSC_HAEIN;  P95354, ARSC_NEIGO;  
P63621, ARSC_NEIMA;  P63622, ARSC_NEIMB;  P0AB97, ARSC_SHIFL;  
P74984, ARSC_YEREN;  

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